Research team untangles more secrets of intrinsically disordered regions of proteins
Intrinsically disordered regions (IDRs) of proteins, when tethered to folded domains, function either as flexible tails or as linkers between domains. Most IDRs are composed of a mixture of oppositely charged residues. Recent measurements of tethered polyampholytes have shown that arginine- and lysine-rich sequences tend to behave very differently from one another.